NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|519664503|ref|WP_020280402|]
View 

catabolite control protein A [Lentilactobacillus otakiensis]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options Â»

Show site features     Horizontal zoom: Ã—

List of domain hits

Name Accession Description Interval E-value
ccpA super family cl31114
catabolite control protein A; Catabolite control protein A is a LacI family global ...
5-333 0e+00

catabolite control protein A; Catabolite control protein A is a LacI family global transcriptional regulator found in Gram-positive bacteria. CcpA is involved in repressing carbohydrate utilization genes [ex: alpha-amylase (amyE), acetyl-coenzyme A synthase (acsA)] and in activating genes involved in transporting excess carbon from the cell [ex: acetate kinase (ackA), alpha-acetolactate synthase (alsS)]. Additionally, disruption of CcpA in Bacillus megaterium, Staphylococcus xylosus, Lactobacillus casei and Lactocacillus pentosus also decreases growth rate, which suggests CcpA is involved in the regulation of other metabolic pathways. [Regulatory functions, DNA interactions]


The actual alignment was detected with superfamily member TIGR01481:

Pssm-ID: 130546 [Multi-domain]  Cd Length: 329  Bit Score: 519.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503    5 TITIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQLARG 84
Cdd:TIGR01481   1 TVTIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIKRLDYRPNAVARGLASKRTTTVGVIIPDISNIYYAELARG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   85 IDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTPIVFAGSVDEEDLYARVNIDY 164
Cdd:TIGR01481  81 IEDIATMYKYNIILSNSDEDPEKEVQVLNTLLSKQVDGIIFMGGTITEKLREEFSRSPVPVVLAGTVDKENELPSVNIDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  165 VAAVQEEVKNLIDRGNRRVAFVCGPLEQAINGKFRLKGYKQALKSAGIPYDEKLVFETDDTYKTGTLLQPALMAVNATAA 244
Cdd:TIGR01481 161 KQATKEAVGELIAKGHKSIAFVGGPLSDSINGEDRLEGYKEALNKAGIQFGEDLVCEGKYSYDAGYKAFAELKGSLPTAV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  245 MVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTKLMHNEPVDEKNVLLPY 324
Cdd:TIGR01481 241 FVASDEMAAGILNAAMDAGIKVPEDLEVITSNNTRLTEMVRPQLSTIIQPLYDIGAVAMRLLTKYMNDEELEEKTVVLPH 320

                  ....*....
gi 519664503  325 GLMKRESTK 333
Cdd:TIGR01481 321 GIELRGSTK 329
 
Name Accession Description Interval E-value
ccpA TIGR01481
catabolite control protein A; Catabolite control protein A is a LacI family global ...
5-333 0e+00

catabolite control protein A; Catabolite control protein A is a LacI family global transcriptional regulator found in Gram-positive bacteria. CcpA is involved in repressing carbohydrate utilization genes [ex: alpha-amylase (amyE), acetyl-coenzyme A synthase (acsA)] and in activating genes involved in transporting excess carbon from the cell [ex: acetate kinase (ackA), alpha-acetolactate synthase (alsS)]. Additionally, disruption of CcpA in Bacillus megaterium, Staphylococcus xylosus, Lactobacillus casei and Lactocacillus pentosus also decreases growth rate, which suggests CcpA is involved in the regulation of other metabolic pathways. [Regulatory functions, DNA interactions]


Pssm-ID: 130546 [Multi-domain]  Cd Length: 329  Bit Score: 519.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503    5 TITIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQLARG 84
Cdd:TIGR01481   1 TVTIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIKRLDYRPNAVARGLASKRTTTVGVIIPDISNIYYAELARG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   85 IDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTPIVFAGSVDEEDLYARVNIDY 164
Cdd:TIGR01481  81 IEDIATMYKYNIILSNSDEDPEKEVQVLNTLLSKQVDGIIFMGGTITEKLREEFSRSPVPVVLAGTVDKENELPSVNIDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  165 VAAVQEEVKNLIDRGNRRVAFVCGPLEQAINGKFRLKGYKQALKSAGIPYDEKLVFETDDTYKTGTLLQPALMAVNATAA 244
Cdd:TIGR01481 161 KQATKEAVGELIAKGHKSIAFVGGPLSDSINGEDRLEGYKEALNKAGIQFGEDLVCEGKYSYDAGYKAFAELKGSLPTAV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  245 MVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTKLMHNEPVDEKNVLLPY 324
Cdd:TIGR01481 241 FVASDEMAAGILNAAMDAGIKVPEDLEVITSNNTRLTEMVRPQLSTIIQPLYDIGAVAMRLLTKYMNDEELEEKTVVLPH 320

                  ....*....
gi 519664503  325 GLMKRESTK 333
Cdd:TIGR01481 321 GIELRGSTK 329
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
65-331 1.49e-129

ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; Ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380521 [Multi-domain]  Cd Length: 268  Bit Score: 370.47  E-value: 1.49e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd06298    1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFKRSPVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAINGKFRLKGYKQALKSAGIPYDEKLVFETDD 224
Cdd:cd06298   81 VVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYINNDKKLQGYKRALEEAGLEFNEPLIFEGDY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 225 TYKTGTLLQPALMAVN-ATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAM 303
Cdd:cd06298  161 DYDSGYELYEELLESGePDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDIGAVAM 240
                        250       260
                 ....*....|....*....|....*...
gi 519664503 304 RLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd06298  241 RLLTKLMNKEEVEETIVKLPHSIIWRQS 268
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
3-333 2.68e-117

DNA-binding transcriptional regulator, LacI/PurR family [Transcription];


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 341.79  E-value: 2.68e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   3 KQTITIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQLA 82
Cdd:COG1609    1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  83 RGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTPIVFAGSVDEEDLYARVNI 162
Cdd:COG1609   81 RGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 163 DYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAiNGKFRLKGYKQALKSAGIPYDEKLVFETDDTYKTG-----TLLQpalM 237
Cdd:COG1609  161 DNRAGARLATEHLIELGHRRIAFIGGPADSS-SARERLAGYREALAEAGLPPDPELVVEGDFSAESGyeaarRLLA---R 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 238 AVNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTKLMHNEPVDE 317
Cdd:COG1609  237 GPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPP 316
                        330
                 ....*....|....*.
gi 519664503 318 KNVLLPYGLMKRESTK 333
Cdd:COG1609  317 ERVLLPPELVVRESTA 332
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
32-332 6.45e-52

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 173.64  E-value: 6.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  32 VKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKV 111
Cdd:PRK11041   4 VSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 112 LNTLLSKQVDGIIFMGNEINGKLREEFKRTKTPIVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPlE 191
Cdd:PRK11041  84 VNLIITKQIDGMLLLGSRLPFDASKEEQRNLPPMVMANEFAPELELPTVHIDNLTAAFEAVNYLHELGHKRIACIAGP-E 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 192 QAINGKFRLKGYKQALKSAGIPYDEKLVFETDDTYKTGTLLQPALMAVNA--TAAMVTDDELAAGIMNGMSDADVKVPDD 269
Cdd:PRK11041 163 EMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQppTAVFCHSDVMALGALSQAKRMGLRVPQD 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 519664503 270 FEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTKLMHNEPVDEKNVLLPYGLMKREST 332
Cdd:PRK11041 243 LSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGST 305
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
6-75 6.94e-33

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 116.53  E-value: 6.94e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503     6 ITIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTN 75
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
175-332 2.62e-26

Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433159 [Multi-domain]  Cd Length: 160  Bit Score: 102.03  E-value: 2.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  175 LIDRGNRRVAFVC--GPLEQAINGKfRLKGYKQALKSAGIPYDEKLVFETDDTYKTGTLLQPALMAVNATAAMVTDDELA 252
Cdd:pfam13377   2 LAELGHRRIALIGpeGDRDDPYSDL-RERGFREAARELGLDVEPTLYAGDDEAEAAAARERLRWLGALPTAVFVANDEVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  253 AGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTKLMHNEPVDEKNVLLPYGLMKREST 332
Cdd:pfam13377  81 LGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVEREST 160
 
Name Accession Description Interval E-value
ccpA TIGR01481
catabolite control protein A; Catabolite control protein A is a LacI family global ...
5-333 0e+00

catabolite control protein A; Catabolite control protein A is a LacI family global transcriptional regulator found in Gram-positive bacteria. CcpA is involved in repressing carbohydrate utilization genes [ex: alpha-amylase (amyE), acetyl-coenzyme A synthase (acsA)] and in activating genes involved in transporting excess carbon from the cell [ex: acetate kinase (ackA), alpha-acetolactate synthase (alsS)]. Additionally, disruption of CcpA in Bacillus megaterium, Staphylococcus xylosus, Lactobacillus casei and Lactocacillus pentosus also decreases growth rate, which suggests CcpA is involved in the regulation of other metabolic pathways. [Regulatory functions, DNA interactions]


Pssm-ID: 130546 [Multi-domain]  Cd Length: 329  Bit Score: 519.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503    5 TITIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQLARG 84
Cdd:TIGR01481   1 TVTIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIKRLDYRPNAVARGLASKRTTTVGVIIPDISNIYYAELARG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   85 IDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTPIVFAGSVDEEDLYARVNIDY 164
Cdd:TIGR01481  81 IEDIATMYKYNIILSNSDEDPEKEVQVLNTLLSKQVDGIIFMGGTITEKLREEFSRSPVPVVLAGTVDKENELPSVNIDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  165 VAAVQEEVKNLIDRGNRRVAFVCGPLEQAINGKFRLKGYKQALKSAGIPYDEKLVFETDDTYKTGTLLQPALMAVNATAA 244
Cdd:TIGR01481 161 KQATKEAVGELIAKGHKSIAFVGGPLSDSINGEDRLEGYKEALNKAGIQFGEDLVCEGKYSYDAGYKAFAELKGSLPTAV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  245 MVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTKLMHNEPVDEKNVLLPY 324
Cdd:TIGR01481 241 FVASDEMAAGILNAAMDAGIKVPEDLEVITSNNTRLTEMVRPQLSTIIQPLYDIGAVAMRLLTKYMNDEELEEKTVVLPH 320

                  ....*....
gi 519664503  325 GLMKRESTK 333
Cdd:TIGR01481 321 GIELRGSTK 329
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
65-331 1.49e-129

ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; Ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380521 [Multi-domain]  Cd Length: 268  Bit Score: 370.47  E-value: 1.49e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd06298    1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFKRSPVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAINGKFRLKGYKQALKSAGIPYDEKLVFETDD 224
Cdd:cd06298   81 VVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYINNDKKLQGYKRALEEAGLEFNEPLIFEGDY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 225 TYKTGTLLQPALMAVN-ATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAM 303
Cdd:cd06298  161 DYDSGYELYEELLESGePDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDIGAVAM 240
                        250       260
                 ....*....|....*....|....*...
gi 519664503 304 RLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd06298  241 RLLTKLMNKEEVEETIVKLPHSIIWRQS 268
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
3-333 2.68e-117

DNA-binding transcriptional regulator, LacI/PurR family [Transcription];


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 341.79  E-value: 2.68e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   3 KQTITIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQLA 82
Cdd:COG1609    1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  83 RGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTPIVFAGSVDEEDLYARVNI 162
Cdd:COG1609   81 RGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 163 DYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAiNGKFRLKGYKQALKSAGIPYDEKLVFETDDTYKTG-----TLLQpalM 237
Cdd:COG1609  161 DNRAGARLATEHLIELGHRRIAFIGGPADSS-SARERLAGYREALAEAGLPPDPELVVEGDFSAESGyeaarRLLA---R 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 238 AVNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTKLMHNEPVDE 317
Cdd:COG1609  237 GPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPP 316
                        330
                 ....*....|....*.
gi 519664503 318 KNVLLPYGLMKRESTK 333
Cdd:COG1609  317 ERVLLPPELVVRESTA 332
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
65-331 7.57e-85

ligand-binding domain of putative DNA transcription regulators highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380630 [Multi-domain]  Cd Length: 269  Bit Score: 257.10  E-value: 7.57e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd19975    1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKQLLKNMNIP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAINGKFRLKGYKQALKSAGIPYDEKLVFETDD 224
Cdd:cd19975   81 VVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDDPNAGYPRYEGYKKALKDAGLPIKENLIVEGDF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 225 TYKTG-----TLLQPALMavnATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIG 299
Cdd:cd19975  161 SFKSGyqamkRLLKNKKL---PTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEMG 237
                        250       260       270
                 ....*....|....*....|....*....|..
gi 519664503 300 AVAMRLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd19975  238 KKAVELLLDLIKNEKKEEKSIVLPHQIIERES 269
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
65-327 3.46e-75

ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily; Ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. In most cases, ligands are monosaccharide including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the domain sugar binding changes the DNA binding activity of the repressor domain.


Pssm-ID: 380491 [Multi-domain]  Cd Length: 264  Bit Score: 232.02  E-value: 3.46e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd06267    1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAGIP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAInGKFRLKGYKQALKSAGIPYDEKLVFETDD 224
Cdd:cd06267   81 VVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLST-SRERLEGYRDALAEAGLPVDPELVVEGDF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 225 TYKTG-----TLLQpalMAVNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIG 299
Cdd:cd06267  160 SEESGyeaarELLA---LPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMG 236
                        250       260
                 ....*....|....*....|....*...
gi 519664503 300 AVAMRLLTKLMHNEPVDEKNVLLPYGLM 327
Cdd:cd06267  237 RAAAELLLERIEGEEEPPRRIVLPTELV 264
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
65-331 4.61e-67

ligand-binding domain of putative DNA transcription regulators highly similar to that of the transcription regulator DegA; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the transcription regulator DegA, which is involved in the control of degradation of Bacillus subtilis amidophosphoribosyltransferase (purF). This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380631 [Multi-domain]  Cd Length: 268  Bit Score: 211.34  E-value: 4.61e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFM-GNEINGKLREEFKRTKT 143
Cdd:cd19976    1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIAsSNISDEAIIKLLKEEKI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 144 PIVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAINGKfRLKGYKQALKSAGIPYDEKLVFETD 223
Cdd:cd19976   81 PVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHE-RIEGYKNALQDHNLPIDESWIYSGE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 224 DTYKTGTLLQPALMAVN-ATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVA 302
Cdd:cd19976  160 SSLEGGYKAAEELLKSKnPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQEA 239
                        250       260
                 ....*....|....*....|....*....
gi 519664503 303 MRLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd19976  240 AKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
65-331 7.11e-65

ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380507 [Multi-domain]  Cd Length: 267  Bit Score: 205.85  E-value: 7.11e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTkTP 144
Cdd:cd06284    1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELLSELSKR-YP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGS-VDEEDLyARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAINGKfRLKGYKQALKSAGIPYDEKLVFETD 223
Cdd:cd06284   80 IVQCCEyIPDSGV-PSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARE-RLEGYRRALAEAGLPVDEDLIIEGD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 224 DTYKTGTLLQPALMAVN--ATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAV 301
Cdd:cd06284  158 FSFEAGYAAARALLALPerPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGET 237
                        250       260       270
                 ....*....|....*....|....*....|
gi 519664503 302 AMRLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd06284  238 AAELLLEKIEGEGVPPEHIILPHELIVRES 267
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
65-331 1.97e-58

ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380514 [Multi-domain]  Cd Length: 264  Bit Score: 189.27  E-value: 1.97e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFM-GNEINgklrEEFKRTKT 143
Cdd:cd06291    1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGsHSLDI----EEYKKLNI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 144 PIVFAGSVDEEDLYArVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEqAINGKFRLKGYKQALKSAGIPYDEKLVFETD 223
Cdd:cd06291   77 PIVSIDRYLSEGIPS-VSSDNYQGGRLAAEHLIEKGCKKILHIGGPSN-NSPANERYRGFEDALKEAGIEYEIIEIDEND 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 224 DTYKTGTLLQPALMA--VNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAV 301
Cdd:cd06291  155 FSEEDAYELAKELLEkyPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAKE 234
                        250       260       270
                 ....*....|....*....|....*....|
gi 519664503 302 AMRLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd06291  235 AVELLLKLIEGEEIEESRIVLPVELIERET 264
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
65-329 3.47e-57

ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380503 [Multi-domain]  Cd Length: 266  Bit Score: 185.93  E-value: 3.47e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd06280    1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRELKRLLKHGIP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFagsVDEE----DLYArVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAINGKfRLKGYKQALKSAGIPYDEKLVF 220
Cdd:cd06280   81 IVL---IDREveglELDL-VAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRE-RLAGYREALAEAGIPVDESLIF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 221 ETDDTYKTGTLLQPALMAVNA--TAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDI 298
Cdd:cd06280  156 EGDSTIEGGYEAVKALLDLPPrpTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEI 235
                        250       260       270
                 ....*....|....*....|....*....|.
gi 519664503 299 GAVAMRLLTKLMHNEPVDEKNVLLPYGLMKR 329
Cdd:cd06280  236 GRIAAQLLLERIEGQGEEPRRIVLPTELIIR 266
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
65-331 2.71e-54

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380513 [Multi-domain]  Cd Length: 267  Bit Score: 178.58  E-value: 2.71e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKrTKTP 144
Cdd:cd06290    1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLKLLA-EGIP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQaINGKFRLKGYKQALKSAGIPYDEKLVFETDD 224
Cdd:cd06290   80 VVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDH-PDAQERYAGYRRALEDAGLEVDPRLIVEGDF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 225 TYKTGTLLQPALMA--VNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVA 302
Cdd:cd06290  159 TEESGYEAMKKLLKrgGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKTA 238
                        250       260
                 ....*....|....*....|....*....
gi 519664503 303 MRLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd06290  239 AEILLELIEGKGRPPRRIILPTELVIRES 267
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
65-321 3.28e-53

periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its close homologs; This group includes the ligand-binding domain of putative repressor of the endoglucanase operon from Paenibacillus polymyxa and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380632 [Multi-domain]  Cd Length: 264  Bit Score: 175.80  E-value: 3.28e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd19977    1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDLIEKLVKSGIP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFagsVD---EEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQaINGKFRLKGYKQALKSAGIPYDEKLV-- 219
Cdd:cd19977   81 VVF---VDryiPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLEL-STRQERLEGYKAALADHGLPVDEELIkh 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 220 -FETDDTYK-TGTLLQpalMAVNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYD 297
Cdd:cd19977  157 vDRQDDVRKaISELLK---LEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYE 233
                        250       260
                 ....*....|....*....|....
gi 519664503 298 IGAVAMRLLTKLMHNEPVDEKNVL 321
Cdd:cd19977  234 IGRKAAELLLDRIENKPKGPPRQI 257
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
32-332 6.45e-52

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 173.64  E-value: 6.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  32 VKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKV 111
Cdd:PRK11041   4 VSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 112 LNTLLSKQVDGIIFMGNEINGKLREEFKRTKTPIVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPlE 191
Cdd:PRK11041  84 VNLIITKQIDGMLLLGSRLPFDASKEEQRNLPPMVMANEFAPELELPTVHIDNLTAAFEAVNYLHELGHKRIACIAGP-E 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 192 QAINGKFRLKGYKQALKSAGIPYDEKLVFETDDTYKTGTLLQPALMAVNA--TAAMVTDDELAAGIMNGMSDADVKVPDD 269
Cdd:PRK11041 163 EMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQppTAVFCHSDVMALGALSQAKRMGLRVPQD 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 519664503 270 FEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTKLMHNEPVDEKNVLLPYGLMKREST 332
Cdd:PRK11041 243 LSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGST 305
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
65-332 5.56e-50

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380508 [Multi-domain]  Cd Length: 269  Bit Score: 167.40  E-value: 5.56e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd06285    1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAARGVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLeQAINGKFRLKGYKQALKSAGIPYDEKLVFETDD 224
Cdd:cd06285   81 VVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPL-NASTGRDRLRGYRRALAEAGLPVPDERIVPGGF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 225 TYKTGTLLQPALMAVNA--TAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVA 302
Cdd:cd06285  160 TIEAGREAAYRLLSRPErpTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRRA 239
                        250       260       270
                 ....*....|....*....|....*....|
gi 519664503 303 MRLLTKLMHNEPVDEKNVLLPYGLMKREST 332
Cdd:cd06285  240 AELLLQLIEGGGRPPRSITLPPELVVREST 269
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
65-330 1.98e-48

ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalS is a dimeric protein like GalR,and its major role is in regulating expression of the high-affinity galactose transporter encoded by the mgl operon, whereas GalR is the exclusive regulator of galactose permease, the low-affinity galactose transporter. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are homologous to the periplasmic sugar binding of ABC-type transport systems.


Pssm-ID: 380494 [Multi-domain]  Cd Length: 266  Bit Score: 163.46  E-value: 1.98e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd06270    1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIPP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLeQAINGKFRLKGYKQALKSAGIPYDEKLVFETDD 224
Cdd:cd06270   81 LVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPL-DIPDARERLAGYRDALAEAGIPLDPSLIIEGDF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 225 TYKTG-----TLL---QP--ALMAVNataamvtdDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQP 294
Cdd:cd06270  160 TIEGGyaaakQLLargLPftALFAYN--------DDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYP 231
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 519664503 295 LYDIGAVAMRLLTKLMHNEPVDEKNVLLPYgLMKRE 330
Cdd:cd06270  232 IEEMAQAAAELALNLAYGEPLPISHEFTPT-LIERD 266
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
65-331 9.19e-48

ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum produces significant amounts of L-glutamate directly from cheap sugar and ammonia; This group includes the ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum which has a unique ability to produce significant amounts of L-glutamate directly from cheap sugar and ammonia. This regulatory protein is a member of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380522 [Multi-domain]  Cd Length: 268  Bit Score: 161.68  E-value: 9.19e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd06299    1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENSEGLQALIAQGLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFagsVDEE-DLYARVNI---DYVAAVQEEVKNLIDRGNRRVAFVCGPLeQAINGKFRLKGYKQALKSAGIPYDEKLVF 220
Cdd:cd06299   81 VVF---VDREvEGLGGVPVvtsDNRPGAREAVEYLVSLGHRRIGYISGPL-STSTGRERLAAFRAALTAAGIPIDEELVA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 221 ETDDTYKTGT-----LLQpalMAVNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPL 295
Cdd:cd06299  157 FGDFRQDSGAaaahrLLS---RGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPV 233
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 519664503 296 YDIGAVAMRLLTKLMHNEPvDEKNVLLPYGLMKRES 331
Cdd:cd06299  234 ERIGRRAVELLLALIENGG-RATSIRVPTELIPRES 268
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
10-331 1.01e-47

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 163.33  E-value: 1.01e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  10 DVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQLARGIDDVA 89
Cdd:PRK10423   3 DVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVERSC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  90 TMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKT-PIV------FAGSVDE-ED---LYA 158
Cdd:PRK10423  83 FERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREIMQRYPSvPTVmmdwapFDGDSDLiQDnslLGG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 159 RVNIDYvaavqeevknLIDRGNRRVAFVCGPLEQAiNGKFRLKGYKQALKSAGIPYDEKLVFETDDTYKTGTLLQPALMA 238
Cdd:PRK10423 163 DLATQY----------LIDKGYTRIACITGPLDKT-PARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLLA 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 239 VNA--TAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTKLMHNEPVD 316
Cdd:PRK10423 232 LPLrpQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQ 311
                        330
                 ....*....|....*
gi 519664503 317 EKNVLLPYGLMKRES 331
Cdd:PRK10423 312 QQRLQLTPELMERGS 326
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
65-331 2.80e-47

ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380511 [Multi-domain]  Cd Length: 268  Bit Score: 160.41  E-value: 2.80e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDV-TNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIF--MGNEINGKLREEfkrT 141
Cdd:cd06288    1 TIGLITDDIaTTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYasMHHREVTLPPEL---T 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 142 KTPIVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPlEQAINGKFRLKGYKQALKSAGIPYDEKLV-- 219
Cdd:cd06288   78 DIPLVLLNCFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGP-EDSLATRLRLAGYRAALAEAGIPYDPSLVvh 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 220 --FETDDTYK-TGTLLQpalMAVNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLY 296
Cdd:cd06288  157 gdWGRESGYEaAKRLLS---APDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYY 233
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 519664503 297 DIGAVAMRLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd06288  234 EMGRRAAELLLDGIEGEPPEPGVIRVPCPLIERES 268
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
65-331 2.69e-46

ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators; This group represents the ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of GntR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding, which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380489 [Multi-domain]  Cd Length: 269  Bit Score: 158.04  E-value: 2.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd01575    1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRKLLRAAGIP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAINGKFRLKGYKQALKSAGIPYDEKLVFETDD 224
Cdd:cd01575   81 VVETWDLPDDPIDMAVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSRARQRLEGFRDALAEAGLPLPLVLLVELPS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 225 TYKTGTLLQPALMAVNAT--AAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVA 302
Cdd:cd01575  161 SFALGREALAELLARHPDldAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPRYEIGRKA 240
                        250       260
                 ....*....|....*....|....*....
gi 519664503 303 MRLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd01575  241 AELLLARLEGEEPEPRVVDLGFELVRRES 269
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
65-327 1.72e-45

ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors; This group includes the ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380517 [Multi-domain]  Cd Length: 269  Bit Score: 155.82  E-value: 1.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVT-----NMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFK 139
Cdd:cd06294    1 TIGLVLPSSAeelfqNPFFSEVLRGISQVANENGYSLLLATGNTEEELLEEVKRMVRGRRVDGFILLYSKEDDPLIEYLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 140 RTKTPIVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAINgKFRLKGYKQALKSAGIPYDEKLV 219
Cdd:cd06294   81 EEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVS-IDRLQGYKQALKEAGLPLDDDYI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 220 FETDDTYKTGTLLQPALMAVNA--TAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYD 297
Cdd:cd06294  160 LLLDFSEEDGYDALQELLSKPPppTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDINPYE 239
                        250       260       270
                 ....*....|....*....|....*....|
gi 519664503 298 IGAVAMRLLTKLMHNEPVDEKNVLLPYGLM 327
Cdd:cd06294  240 LGREAAKLLINLLEGPESLPKNVIVPHELI 269
lacI PRK09526
lac repressor; Reviewed
1-332 2.50e-45

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 157.46  E-value: 2.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   1 MDKQTITIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQ 80
Cdd:PRK09526   1 MKSKPVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  81 LARGIDDVATMYKYNIILTNSDSNNEKEVK-VLNTLLSKQVDGIIfmgneINGKLREEFKR------TKTPIVFAgSVDE 153
Cdd:PRK09526  81 IAAAIKSRADQLGYSVVISMVERSGVEACQaAVNELLAQRVSGVI-----INVPLEDADAEkivadcADVPCLFL-DVSP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 154 EDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPlEQAINGKFRLKGYKQALKSAGI-PYDeklVFETDDTYKTGtlL 232
Cdd:PRK09526 155 QSPVNSVSFDPEDGTRLGVEHLVELGHQRIALLAGP-ESSVSARLRLAGWLEYLTDYQLqPIA---VREGDWSAMSG--Y 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 233 QPALMAVNA----TAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTK 308
Cdd:PRK09526 229 QQTLQMLREgpvpSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLA 308
                        330       340
                 ....*....|....*....|....
gi 519664503 309 LMHNEPVdEKNVLLPYGLMKREST 332
Cdd:PRK09526 309 LSQGQAV-KGSQLLPTSLVVRKST 331
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
65-331 3.86e-45

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 155.12  E-value: 3.86e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd06293    1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRARGTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPL--EQAINgkfRLKGYKQALKSAGIPYDEklVFET 222
Cdd:cd06293   81 VVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLrtRQVAE---RLAGARAAVAEAGLDPDE--VVRE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 223 DDTYKTGTLL------QPALMAVNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLY 296
Cdd:cd06293  156 LSAPDANAELgraaaaQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSY 235
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 519664503 297 DIGAVAMRLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd06293  236 ELGRAAADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
65-331 5.32e-44

ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli; Ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. This dimeric PurR belongs to the LacI-GalR family of transcription regulators and is activated to bind to DNA operator sites by initially binding either of high affinity corepressors, hypoxanthine or guanine. PurR is composed of two functional domains: aan N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the purine transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380499 [Multi-domain]  Cd Length: 269  Bit Score: 152.03  E-value: 5.32e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKR-TKT 143
Cdd:cd06275    1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAAlRSI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 144 PIVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAInGKFRLKGYKQALKSAGIPYDEKLVFETD 223
Cdd:cd06275   81 PVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSV-SRERLAGFRRALAEAGIEVPPSWIVEGD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 224 DTYKTGTLLQPALMAVNA--TAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAV 301
Cdd:cd06275  160 FEPEGGYEAMQRLLSQPPrpTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGEL 239
                        250       260       270
                 ....*....|....*....|....*....|
gi 519664503 302 AMRLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd06275  240 AVELLLDRIENKREEPQSIVLEPELIERES 269
PBP1_CcpB-like cd06286
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ...
65-329 5.65e-44

ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species; This group includes the ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species. Catabolite control protein B (CcpB) is 30% identical in sequence to CcpA which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. Like CcpA, the DNA-binding protein CcpB exerts its catabolite-repressing effect by a mechanism dependent on the presence of HPr(Ser-P), the small phosphocarrier proteins of the phosphoenolpyruvate-sugar phosphotransferase system, but with a less significant degree.


Pssm-ID: 380509 [Multi-domain]  Cd Length: 262  Bit Score: 151.54  E-value: 5.65e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIF--MGNEIngklrEEFK--R 140
Cdd:cd06286    1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIItsRENDW-----EVIEpyA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 141 TKTPIVFAGSVDEEDLYArVNIDYVAAVQEEVKNLIDRGNRRVAFVCG-PLEQAINGKFRLKGYKQALKSAGIPYDEKLV 219
Cdd:cd06286   76 KYGPIVLCEETDSPDIPS-VYIDRYEAYLEALEYLKEKGHRKIGYCLGrPESSSASTQARLKAYQDVLGEHGLSLREEWI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 220 FETDDTYKTGTLLQPALMAVNA--TAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMvrPKMSSITQPLYD 297
Cdd:cd06286  155 FTNCHTIEDGYKLAKKLLALKErpDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISEL--LNLTTIDQPLEE 232
                        250       260       270
                 ....*....|....*....|....*....|..
gi 519664503 298 IGAVAMRLLTKLMHNEPVdeKNVLLPYGLMKR 329
Cdd:cd06286  233 MGKEAFELLLSQLESKEP--TKKELPSKLIER 262
PBP1_AglR_RafR-like cd06292
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ...
65-332 8.24e-44

Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the repressors specific raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins highly similar to DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR). Members of this group belong to the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380515 [Multi-domain]  Cd Length: 273  Bit Score: 151.65  E-value: 8.24e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPD----VTNMYFAQLARGIDDVATMYKYNIILTnSDSNNEKEVKVLNTLL-SKQVDGIIFMGNEIN----GKLR 135
Cdd:cd06292    1 LIGYVVPElpggFSDPFFDEFLAALGHAAAARGYDVLLF-TASGDEDEIDYYRDLVrSRRVDGFVLASTRHDdprvRYLH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 136 EEfkrtKTPIVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEqAINGKFRLKGYKQALKSAGIPYD 215
Cdd:cd06292   80 EA----GVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEG-SVPSDDRLAGYRAALEEAGLPFD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 216 EKLVFETDDTYKTGTLLQPALMAVN--ATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQ 293
Cdd:cd06292  155 PGLVVEGENTEEGGYAAAARLLDLGppPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQ 234
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 519664503 294 PLYDIGAVAMRLLTKLMHNEPVDEKNVLLPYGLMKREST 332
Cdd:cd06292  235 PIDEIGRAVVDLLLAAIEGNPSEPREILLQPELVVRESS 273
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
65-331 3.07e-43

ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380483 [Multi-domain]  Cd Length: 274  Bit Score: 150.02  E-value: 3.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMG-----NEINGKLREEFK 139
Cdd:cd01541    1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPtksalPNPNLDLYEELQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 140 RTKTPIVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCgpleQAIN--GKFRLKGYKQALKSAGIPYDEK 217
Cdd:cd01541   81 KKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGIF----KSDDlqGVERYQGFIKALREAGLPIDDD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 218 LVF----ETDDTYKTGTLLQPALMAVN-ATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSIT 292
Cdd:cd01541  157 RILwystEDLEDRFFAEELREFLRRLSrCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTSVV 236
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 519664503 293 QPLYDIGAVAMRLLTKLMhNEPVDEKNVLLPYGLMKRES 331
Cdd:cd01541  237 HPKEELGRKAAELLLRMI-EEGRKPESVIFPPELIERES 274
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
65-331 6.97e-41

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380505 [Multi-domain]  Cd Length: 267  Bit Score: 143.58  E-value: 6.97e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIF-----MGNEINGKLREEfk 139
Cdd:cd06282    1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILtvgdaQGSEALELLEEE-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 140 rtKTPIVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAINGKFRLKGYKQALKSAGipYDEKLV 219
Cdd:cd06282   79 --GVPYVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDFSASDRARLRYQGYRDALKEAG--LKPIPI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 220 FETDDTYktgTLLQPALMAV-----NATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQP 294
Cdd:cd06282  155 VEVDFPT---NGLEEALTSLlsgpnPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQP 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 519664503 295 LYDIGAVAMRLLTKLMHNEPVDeKNVLLPYGLMKRES 331
Cdd:cd06282  232 SRDMGRAAADLLLAEIEGESPP-TSIRLPHHLREGGS 267
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
7-306 8.31e-41

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 145.64  E-value: 8.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   7 TIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQLARGID 86
Cdd:PRK10703   3 TIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  87 DVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFK-RTKTPIVFA--GSVDeEDLYARVnID 163
Cdd:PRK10703  83 KNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMLEeYRHIPMVVMdwGEAK-ADFTDAI-ID 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 164 ------YVAAvqeevKNLIDRGNRRVAFVCGPLEQAInGKFRLKGYKQALKSAGIPYDEKLV----FETDDTYK--TGTL 231
Cdd:PRK10703 161 nafeggYLAG-----RYLIERGHRDIGVIPGPLERNT-GAGRLAGFMKAMEEANIKVPEEWIvqgdFEPESGYEamQQIL 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519664503 232 LQPALmavnATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLL 306
Cdd:PRK10703 235 SQKHR----PTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNML 305
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
65-324 1.21e-39

ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380484 [Multi-domain]  Cd Length: 259  Bit Score: 140.32  E-value: 1.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd01542    1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKALKKLKIP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGSvDEEDLYARVNIDYvAAVQEEVKNLIDRGNRRVAFVCGPLEQAINGKFRLKGYKQALKSAGIpyDEKLVFETDD 224
Cdd:cd01542   81 VVVLGQ-EHEGFSCVYHDDY-GAGKLLGEYLLKKGHKNIAYIGVDEEDIAVGVARKQGYLDALKEHGI--DEVEIVETDF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 225 TYKTGTLLQPALMAVNATAAMV--TdDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVA 302
Cdd:cd01542  157 SMESGYEAAKELLKENKPDAIIcaT-DNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGEKA 235
                        250       260
                 ....*....|....*....|..
gi 519664503 303 MRLLTKLMHNEPVDEKnVLLPY 324
Cdd:cd01542  236 AELLLDMIEGEKVPKK-QKLPY 256
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
65-331 1.87e-38

ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380487 [Multi-domain]  Cd Length: 270  Bit Score: 137.30  E-value: 1.87e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEV-KVLNTLLSKQVDGIIF---MGNeiNGKLREEFKR 140
Cdd:cd01545    1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVEPCDSDDEDLAdRLRRFLSRSRPDGVILtppLSD--DPALLDALDE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 141 TKTPIVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAiNGKFRLKGYKQALKSAGIPYDEKLVF 220
Cdd:cd01545   79 LGIPYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHG-ASAERLEGFRDALAEAGLPLDPDLVV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 221 ETDDTYKTG-----TLL---QP--ALMAVNataamvtdDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSS 290
Cdd:cd01545  158 QGDFTFESGleaaeALLdlpDRptAIFASN--------DEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTT 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 519664503 291 ITQPLYDIGAVAMRLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd01545  230 VRQPIAEMARRAVELLIAAIRGAPAGPERETLPHELVIRES 270
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
6-329 2.33e-38

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 139.07  E-value: 2.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   6 ITIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQLARGI 85
Cdd:PRK10014   7 ITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAGL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  86 DDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEING-KLREEFKRTKTPIVFAG---SVDEEDLyarVN 161
Cdd:PRK10014  87 TEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSdDLREMAEEKGIPVVFASrasYLDDVDT---VR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 162 IDYVAAVQEEVKNLIDRGNRRVAFVCG---PLEQAingkFRLKGYKQALKSAGIPYDEKLVFETDDTYK-----TGTLLQ 233
Cdd:PRK10014 164 PDNMQAAQLLTEHLIRNGHQRIAWLGGqssSLTRA----ERVGGYCATLLKFGLPFHSEWVLECTSSQKqaaeaITALLR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 234 --PALMAV---NATAAM-----VtddeLAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIG-AVA 302
Cdd:PRK10014 240 hnPTISAVvcyNETIAMgawfgL----LRAGRQSGESGVDRYFEQQVALAAFTDVPEAELDDPPLTWASTPAREIGrTLA 315
                        330       340
                 ....*....|....*....|....*..
gi 519664503 303 MRLLTKLMHNEpVDEKNVLLPYGLMKR 329
Cdd:PRK10014 316 DRMMQRITHEE-THSRNLIIPPRLIAR 341
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
65-331 3.73e-38

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380504 [Multi-domain]  Cd Length: 270  Bit Score: 136.60  E-value: 3.73e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIF-MGNEINGKLREEFKRTKT 143
Cdd:cd06281    1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILtPGDEDDPELAAALARLDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 144 PIVFagsVDEE--DLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEqAINGKFRLKGYKQALKSAGIPYDEKLV-- 219
Cdd:cd06281   81 PVVL---IDRDlpGDIDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPD-IRPGRERIAGFKAAFAAAGLPPDPDLVrl 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 220 --FETDDTYKTGTllqpALMAVNA--TAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPL 295
Cdd:cd06281  157 gsFSADSGFREAM----ALLRQPRppTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDL 232
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 519664503 296 YDIGAVAMRLLTKLMHNEPVDE-KNVLLPYGLMKRES 331
Cdd:cd06281  233 DAVGRAAAELLLDRIEGPPAGPpRRIVVPTELILRDS 269
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
65-330 5.75e-38

ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria; This group includes the ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria. They are members of the LacI-GalR family of repressor proteins which are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380512 [Multi-domain]  Cd Length: 268  Bit Score: 136.16  E-value: 5.75e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIF---MGNeiNGKLREEFKRT 141
Cdd:cd06289    1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILspaAGT--TAELLRRLKAW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 142 KTPIVFAG-SVDEEDL-YARvnIDYVAAVQEEVKNLIDRGNRRVAFVcGPLEQAINGKFRLKGYKQALKSAGIPYDEKLV 219
Cdd:cd06289   79 GIPVVLALrDVPGSDLdYVG--IDNRLGAQLATEHLIALGHRRIAFL-GGLSDSSTRRERLAGFRAALAEAGLPLDESLI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 220 FETDDTYKTGTLLQPALMAVN--ATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYD 297
Cdd:cd06289  156 VPGPATREAGAEAARELLDAAppPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPRE 235
                        250       260       270
                 ....*....|....*....|....*....|...
gi 519664503 298 IGAVAMRLLTKLMHNEPVDEKNVLLPYGLMKRE 330
Cdd:cd06289  236 IGRRAARLLLRRIEGPDTPPERIIIEPRLVVRE 268
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
6-305 2.38e-37

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 136.44  E-value: 2.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   6 ITIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQLARGI 85
Cdd:PRK10401   2 ITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  86 DDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTPIVFAGSVDEEDLYARVNIDYV 165
Cdd:PRK10401  82 DLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDQIPGMVLINRVVPGYAHRCVCLDNV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 166 AAVQEEVKNLIDRGNRRVAFVCG--PLEqaiNGKFRLKGYKQALKSAGIPYDEKLVFETDDTYKTGTLLQPALMAVNA-- 241
Cdd:PRK10401 162 SGARMATRMLLNNGHQRIGYLSSshGIE---DDAMRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELLGRNLql 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 519664503 242 TAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRL 305
Cdd:PRK10401 239 TAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATEL 302
PRK10727 PRK10727
HTH-type transcriptional regulator GalR;
7-331 4.02e-37

HTH-type transcriptional regulator GalR;


Pssm-ID: 182681 [Multi-domain]  Cd Length: 343  Bit Score: 136.04  E-value: 4.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   7 TIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQLARGID 86
Cdd:PRK10727   3 TIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  87 DVATMYKYNIILTNSDSNNEKEVKVLNTL----------------------LSKQVDGIIFmgneINGKLREEFKRtktp 144
Cdd:PRK10727  83 QVAYHTGNFLLIGNGYHNEQKERQAIEQLirhrcaalvvhakmipdaelasLMKQIPGMVL----INRILPGFENR---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 ivfagSVDEEDLYARvnidYVAavqeeVKNLIDRGNRRVAFVCG--PLEQAINgkfRLKGYKQALKSAGIPYDEKLVF-- 220
Cdd:PRK10727 155 -----CIALDDRYGA----WLA-----TRHLIQQGHTRIGYLCSnhSISDAED---RLQGYYDALAESGIPANDRLVTfg 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 221 ETDDTYKTGTLLQPALMAVNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGA 300
Cdd:PRK10727 218 EPDESGGEQAMTELLGRGRNFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMAT 297
                        330       340       350
                 ....*....|....*....|....*....|.
gi 519664503 301 VAMRLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:PRK10727 298 QAAELALALADNRPLPEITNVFSPTLVRRHS 328
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
65-331 6.20e-37

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380497 [Multi-domain]  Cd Length: 268  Bit Score: 133.40  E-value: 6.20e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd06273    1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDPELFELLEQRQVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLE-----QAingkfRLKGYKQALKSAGIPYDEKLV 219
Cdd:cd06273   81 YVLTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAgndraRA-----RLAGIRDALAERGLELPEERV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 220 FETDDTYKTGTLLQPALMAVN--ATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYD 297
Cdd:cd06273  156 VEAPYSIEEGREALRRLLARPprPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPARE 235
                        250       260       270
                 ....*....|....*....|....*....|....
gi 519664503 298 IGAVAMRLLTKLMHNEPVdEKNVLLPYGLMKRES 331
Cdd:cd06273  236 IGELAARYLLALLEGGPP-PKSVELETELIVRES 268
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
65-331 1.17e-35

ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of LacI is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380488 [Multi-domain]  Cd Length: 265  Bit Score: 130.01  E-value: 1.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVK-VLNTLLSKQVDGIIFMGNEiNGKLREEFKRTK- 142
Cdd:cd01574    1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVDEDDPASVReALDRLLSQRVDGIIVIAPD-EAVLEALRRLPPg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 143 TPIVFAGSVDEEDLyARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLE--QAINgkfRLKGYKQALKSAGIPYDEklVF 220
Cdd:cd01574   80 LPVVIVGSGPSPGV-PTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDwvDARA---RLRGWREALEEAGLPPPP--VV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 221 ETDDTYKTG-----TLLQpalmAVNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPL 295
Cdd:cd01574  154 EGDWSAASGyragrRLLD----DGPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDF 229
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 519664503 296 YDIGAVAMRLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd01574  230 AELGRRAVELLLALIEGPAPPPESVLLPPELVVRES 265
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
77-331 2.30e-35

ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalR is a dimeric protein like GalS and is exclusively involved in the regulation of galactose permease, the low-affinity galactose transporter. GalS is involved in regulating expression of the high-affinity galactose transporter encoded by the mgl operon. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are structurally homologous to the periplasmic sugar binding of ABC-type transport systems.


Pssm-ID: 380486 [Multi-domain]  Cd Length: 269  Bit Score: 129.18  E-value: 2.30e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  77 YFAQLARGIDDVATMYKYNIILTNSDSNNEKEvkvlntlLSKQVDGIIFMGNeINGKLREEFKRTKTPIVFAGSVDEEDL 156
Cdd:cd01544   18 YYLSIRLGIEKEAKKLGYEIKTIFRDDEDLES-------LLEKVDGIIAIGK-FSKEEIEKLKKLNPNIVFVDSNPDPDG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 157 YARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGpLEQAINGK-----FRLKGYKQALKSAGiPYDEKLVFETDDTYKTG-T 230
Cdd:cd01544   90 FDSVVPDFEQAVRQALDYLIELGHRRIGFIGG-KEYTSDDGeeiedPRLRAFREYMKEKG-LYNEEYIYIGEFSVESGyE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 231 LLQPALMAVN-ATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTKL 309
Cdd:cd01544  168 AMKELLKEGDlPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMGRTAVRLLLER 247
                        250       260
                 ....*....|....*....|..
gi 519664503 310 MHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd01544  248 INGGRTIPKKVLLPTKLIERES 269
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
65-332 1.19e-34

ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation; This group includes the ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation. This group belongs to the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380519 [Multi-domain]  Cd Length: 270  Bit Score: 127.39  E-value: 1.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd06296    1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSAGIP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVF---AGSVDEEDLyaRVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPlEQAINGKFRLKGYKQALKSAGIPYDEKLVFE 221
Cdd:cd06296   81 FVLidpVGEPDPDLP--SVGATNWAGGRLATEHLLDLGHRRIAVITGP-PRSVSGRARLAGYRAALAEAGIAVDPDLVRE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 222 TDDTYKTGTLLQPAL--MAVNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIG 299
Cdd:cd06296  158 GDFTYEAGYRAARELleLPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREMG 237
                        250       260       270
                 ....*....|....*....|....*....|...
gi 519664503 300 AVAMRLLTKLMHNEPVDEKNVLLPYGLMKREST 332
Cdd:cd06296  238 AVAVRLLLRLLEGGPPDARRIELATELVVRGST 270
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
6-75 6.94e-33

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 116.53  E-value: 6.94e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503     6 ITIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTN 75
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
65-323 4.46e-32

ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR; Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380506 [Multi-domain]  Cd Length: 266  Bit Score: 120.35  E-value: 4.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd06283    1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNNDAYLELAQKGLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFagsVD---EEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEqAINGKF-RLKGYKQALKSAGIPYDEkLVF 220
Cdd:cd06283   81 VVL---VDrqiEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIK-GISTRReRLQGFLDALARYNIEGDV-YVI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 221 ETDDTYKTGTLLQPALMAVNA--TAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDI 298
Cdd:cd06283  156 EIEDTEDLQQALAAFLSQHDGgkTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEI 235
                        250       260
                 ....*....|....*....|....*
gi 519664503 299 GAVAMRLLTKLMHNEPVDEKNVLLP 323
Cdd:cd06283  236 GKAAAEILLERIEGDSGEPKEIELP 260
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
61-331 5.81e-30

ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators; This group includes the ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. The binding of CelR to the celE promoter is inhibited specifically by cellobiose. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380518 [Multi-domain]  Cd Length: 273  Bit Score: 115.04  E-value: 5.81e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  61 KKTTTVGVIVP-------DVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKevkVLNTLLSKQVDGIIFMGNEINGK 133
Cdd:cd06295    1 QRSRTIAVVVPmdphgdqSITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQ---LARLLDSGRADGLIVLGQGLDHD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 134 LREEFKRTKTPIVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAIngKFRLKGYKQALKSAGIP 213
Cdd:cd06295   78 ALRELAQQGLPMVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPEV--ADRLQGYRDALAEAGLE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 214 YDEKLVFETDDTYKTGTLLQPALMAVNAT--AAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSI 291
Cdd:cd06295  156 ADPSLLLSCDFTEESGYAAMRALLDSGTAfdAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTV 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 519664503 292 TQPLYDIGAVAMRLLTKLMHNEPVDEknVLLPYGLMKRES 331
Cdd:cd06295  236 RQDLALAGRLLVEKLLALIAGEPVTS--SMLPVELVVRES 273
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
1-326 7.53e-29

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 113.58  E-value: 7.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   1 MDKQTITIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQ 80
Cdd:PRK14987   1 MKKKRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  81 LARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTPIVFAGSVDEEDLYARV 160
Cdd:PRK14987  81 VLRGIESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPVVELMDSQSPCLDIAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 161 NIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQaiNGKFRLKGYKQALKSAGI-PYdeKLVFETDDTYKTGTLL--QPALM 237
Cdd:PRK14987 161 GFDNFEAARQMTTAIIARGHRHIAYLGARLDE--RTIIKQKGYEQAMLDAGLvPY--SVMVEQSSSYSSGIELirQARRE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 238 AVNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTKLMHNEPVDE 317
Cdd:PRK14987 237 YPQLDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESVTP 316

                 ....*....
gi 519664503 318 KNVLLPYGL 326
Cdd:PRK14987 317 KMLDLGFTL 325
PBP1_LacI-like cd06277
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
77-331 1.82e-27

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380500 [Multi-domain]  Cd Length: 275  Bit Score: 108.48  E-value: 1.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  77 YFAQLARGIDDVATMYKYNIILTNSDSNNEKEvKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTPIVFAGSVDEEDL 156
Cdd:cd06277   20 FFSELIDGIEREARKYGYNLLISSVDIGDDFD-EILKELTDDQSSGIILLGTELEEKQIKLFQDVSIPVVVVDNYFEDLN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 157 YARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAiNGKFRLKGYKQALKSAGIPYDEKLVFETDDTYKTGTLLQPAL 236
Cdd:cd06277   99 FDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIK-NFEERRRGFRKAMRELGLSEDPEPEFVVSVGPEGAYKDMKAL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 237 MAVNA---TAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTKLMHNE 313
Cdd:cd06277  178 LDTGPklpTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKIKDP 257
                        250
                 ....*....|....*...
gi 519664503 314 PVDEKNVLLPYGLMKRES 331
Cdd:cd06277  258 DGGTLKILVSTKLVERGS 275
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
65-326 3.63e-27

Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380665 [Multi-domain]  Cd Length: 269  Bit Score: 107.64  E-value: 3.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVP----DVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEkEVKVLNTLL-SKQVDGIIfmgneINGKLREEF- 138
Cdd:cd20010    1 AIGLVLPldpgDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGED-ELATYRRLVeRGRVDGFI-----LARTRVNDPr 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 139 ----KRTKTPIVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAiNGKFRLKGYKQALKSAGIPY 214
Cdd:cd20010   75 iaylLERGIPFVVHGRSESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELN-FAHQRRDGYRAALAEAGLPV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 215 DEKLVFETDDTYKTGTLLQPALMAVNA--TAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTK-LTEMVRPKMSSI 291
Cdd:cd20010  154 DPALVREGPLTEEGGYQAARRLLALPPppTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLpALEYFSPPLTTT 233
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 519664503 292 TQPLYDIGAVAMRLLTKLMHNEPVDEKNVLLPYGL 326
Cdd:cd20010  234 RSSLRDAGRRLAEMLLALIDGEPAAELQELWPPEL 268
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
65-331 4.48e-27

ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380502 [Multi-domain]  Cd Length: 284  Bit Score: 107.68  E-value: 4.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPD-----VTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLlskqVDGIIFMGNEINGKLREEFK 139
Cdd:cd06279    1 AIGVLLPDdlsyaFSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAAAVRNAA----VDGFIVYGLSDDDPAVAALR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 140 RTKTPIVFAGSVDEEDLYArVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAINGKF----------------RLKGY 203
Cdd:cd06279   77 RRGLPLVVVDGPAPPGIPS-VGIDDRAAARAAARHLLDLGHRRIAILSLRLDRGRERGPvsaerlaaatnsvareRLAGY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 204 KQALKSAGIPYDEKLVFETDDTYKTGTllQPALMAV-----NATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDT 278
Cdd:cd06279  156 RDALEEAGLDLDDVPVVEAPGNTEEAG--RAAARALlaldpRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDDI 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 519664503 279 KLTEMVRPKMSSITQPLYDIGAVAMRLLTKLMHNEPVDEknVLLPYGLMKRES 331
Cdd:cd06279  234 PEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPGAPPRP--VILPTELVVRAS 284
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
175-332 2.62e-26

Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433159 [Multi-domain]  Cd Length: 160  Bit Score: 102.03  E-value: 2.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  175 LIDRGNRRVAFVC--GPLEQAINGKfRLKGYKQALKSAGIPYDEKLVFETDDTYKTGTLLQPALMAVNATAAMVTDDELA 252
Cdd:pfam13377   2 LAELGHRRIALIGpeGDRDDPYSDL-RERGFREAARELGLDVEPTLYAGDDEAEAAAARERLRWLGALPTAVFVANDEVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  253 AGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTKLMHNEPVDEKNVLLPYGLMKREST 332
Cdd:pfam13377  81 LGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVEREST 160
fruct_sucro_rep TIGR02417
D-fructose-responsive transcription factor; Members of this family belong the lacI ...
7-210 3.40e-26

D-fructose-responsive transcription factor; Members of this family belong the lacI helix-turn-helix family (pfam00356) of DNA-binding transcriptional regulators. All members are from the proteobacteria. Characterized members act as positive and negative transcriptional regulators of fructose and sucrose transport and metabolism. Sucrose is a disaccharide composed of fructose and glucose; D-fructose-1-phosphate rather than an intact sucrose moiety has been shown to act as the inducer. [Regulatory functions, DNA interactions]


Pssm-ID: 131470 [Multi-domain]  Cd Length: 327  Bit Score: 105.99  E-value: 3.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503    7 TIYDVAREASVSMATVSRVVNGNAN---VKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQLAR 83
Cdd:TIGR02417   1 TLSDIAKLAGVSKTTASYVINGKAKeyrISQETVERVMAVVREQGYQPNIHAASLRAGRSRTIGLVIPDLENYSYARIAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   84 GIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIF-----MGNEINGKLREEfkrtKTPIV-FAGSVDEEDLY 157
Cdd:TIGR02417  81 ELEQQCREAGYQLLIACSDDNPDQEKVVIENLLARQVDALIVascmpPEDAYYQKLQNE----GLPVVaLDRSLDDEHFC 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 519664503  158 ARVNIDyVAAVQEEVKNLIDRGNRRVAFVcGPLEQAINGKFRLKGYKQALKSA 210
Cdd:TIGR02417 157 SVISDD-VDAAAELIERLLSQHADEFWYL-GAQPELSVSRDRLAGFRQALKQA 207
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
65-331 6.13e-26

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380501 [Multi-domain]  Cd Length: 266  Bit Score: 104.15  E-value: 6.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDsNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd06278    1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVD-DEDDVDDALRQLLQYRVDGVIVTSATLSSELAEECARRGIP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPlEQAINGKFRLKGYKQALKSAGIPYDEklVFETDD 224
Cdd:cd06278   80 VVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGP-EGTSTSRERERGFRAALAELGLPPPA--VEAGDY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 225 TYKTG-----TLLQpalMAVNATAAMVTDDELAAGIMNGM-SDADVKVPDDFEIITSNDTKLTEmvRP--KMSSITQPLY 296
Cdd:cd06278  157 SYEGGyeaarRLLA---APDRPDAIFCANDLMALGALDAArQEGGLVVPEDISVVGFDDIPMAA--WPsyDLTTVRQPIE 231
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 519664503 297 DIGAVAMRLLTKLMHNEPVDEKNVLLPYGLMKRES 331
Cdd:cd06278  232 EMAEAAVDLLLERIENPETPPERRVLPGELVERGS 266
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
115-332 8.99e-26

ligand-binding domain of DNA transcription repressor specific for xylose (XylR); Ligand-binding domain of DNA transcription repressor specific for xylose (XylR), a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of XylR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380485 [Multi-domain]  Cd Length: 265  Bit Score: 103.44  E-value: 8.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 115 LLSKQVDGIIfmGNEINGKLREEFKRTKTPIVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFvCGPLeqai 194
Cdd:cd01543   46 LKGWKGDGII--ARLDDPELAEALRRLGIPVVNVSGSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAF-CGFR---- 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 195 NGKF---RLKGYKQALKSAGIP---YDEKLVFETDDTYKTGTLL------QP---ALMAVNataamvtdDELAAGIMNGM 259
Cdd:cd01543  119 NAAWsreRGEGFREALREAGYEchvYESPPSGSSRSWEEEREELadwlksLPkpvGIFACN--------DDRARQVLEAC 190
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519664503 260 SDADVKVPDDFEII-TSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLTKLMHNEPVDEKNVLL-PYGLMKREST 332
Cdd:cd01543  191 REAGIRVPEEVAVLgVDNDELICELSSPPLSSIALDAEQIGYEAAELLDRLMRGERVPPEPILIpPLGVVTRQST 265
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
65-331 1.42e-23

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380629 [Multi-domain]  Cd Length: 270  Bit Score: 97.62  E-value: 1.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPD---VTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGnEINGKLREEFKRT 141
Cdd:cd19974    1 NIAVLIPErffGDNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILG-EISKEYLEKLKEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 142 KTPIVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVcGPLEQAINGKFRLKGYKQALKSAGIPYDEK-LVF 220
Cdd:cd19974   80 GIPVVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFV-GDINYTSSFMDRYLGYRKALLEAGLPPEKEeWLL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 221 ETDDTYKTGT---LLQPALMAVnaTAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYD 297
Cdd:cd19974  159 EDRDDGYGLTeeiELPLKLMLP--TAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTVEVDKEA 236
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 519664503 298 IGAVAMRLLTKLMHN-EPVDEKnVLLPYGLMKRES 331
Cdd:cd19974  237 MGRRAVEQLLWRIENpDRPFEK-ILVSGKLIERDS 270
PRK11303 PRK11303
catabolite repressor/activator;
10-124 2.12e-23

catabolite repressor/activator;


Pssm-ID: 236897 [Multi-domain]  Cd Length: 328  Bit Score: 98.41  E-value: 2.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  10 DVAREASVSMATVSRVVNGNAN---VKPATRKKVLDVIEKLDYRPNAVARGLASKKTTTVGVIVPDVTNMYFAQLARGID 86
Cdd:PRK11303   5 EIARLAGVSRTTASYVINGKAKqyrVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIAKYLE 84
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 519664503  87 DVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGII 124
Cdd:PRK11303  85 RQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALI 122
PRK10339 PRK10339
DNA-binding transcriptional repressor EbgR; Provisional
7-333 8.94e-23

DNA-binding transcriptional repressor EbgR; Provisional


Pssm-ID: 182389 [Multi-domain]  Cd Length: 327  Bit Score: 96.75  E-value: 8.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   7 TIYDVAREASVSMATVSRVVNGNA--NVKPATRKKVLDVIEKLDYRPNAVARGL-ASKKTTTVGVIVP-----DVTNMYF 78
Cdd:PRK10339   3 TLKDIAIEAGVSLATVSRVLNDDPtlNVKEETKHRILEIAEKLEYKTSSARKLQtGAVNQHHILAIYSyqqelEINDPYY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  79 AQLARGIDdvATMYKYNIILTNS-DSNNEKEVkvlntllsKQVDGIIFMGNEINgKLREEFKRTKTPIVFAGSVDEEDLY 157
Cdd:PRK10339  83 LAIRHGIE--TQCEKLGIELTNCyEHSGLPDI--------KNVTGILIVGKPTP-ALRAAASALTDNICFIDFHEPGSGY 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 158 ARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGP--------LEQAINGKFRLKGYKQalksagipydEKLVFETDDTYKTG 229
Cdd:PRK10339 152 DAVDIDLARISKEIIDFYINQGVNRIGFIGGEdepgkadiREVAFAEYGRLKQVVR----------EEDIWRGGFSSSSG 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 230 TLLQPALMAVN--ATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGAVAMRLLT 307
Cdd:PRK10339 222 YELAKQMLAREdyPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLY 301
                        330       340
                 ....*....|....*....|....*.
gi 519664503 308 KLMHNEPVDEKNVLLPYGLMKRESTK 333
Cdd:PRK10339 302 EKARDGRALPLLVFVPSKLKLRGTTR 327
PBP1_CcpA_TTHA0807 cd06297
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ...
65-314 4.68e-21

ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its close homologs; Ligand-binding domain of the uncharacterized transcription regulator TTHA0807 from the extremely thermophilic organism Thermus thermophilus HB8 and close homologs from other bacteria. Although its exact biological function is not known, the TTHA0807 belongs to the catabolite control protein A (CcpA)family of regulatory proteins. The CcpA functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380520 [Multi-domain]  Cd Length: 268  Bit Score: 90.99  E-value: 4.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd06297    1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMASLDLTELFEEVIVPTEKP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGSvdEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAINGKF---RLKGYKQALKSAGIPYDEKLVFE 221
Cdd:cd06297   81 VVLIDA--NSMGYDCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVFTETVfreREQGFLEALNKAGRPISSSRMFR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 222 TDDTYKTGTLLQPALM--AVNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMvrPKMSSITQPLYDIG 299
Cdd:cd06297  159 IDNSSKKAECLARELLkkADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAAS--PGLTTVRQPVEEMG 236
                        250
                 ....*....|....*
gi 519664503 300 AVAMRLLTKLMhNEP 314
Cdd:cd06297  237 EAAAKLLLKRL-NEY 250
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
9-60 2.38e-20

Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites.


Pssm-ID: 143331 [Multi-domain]  Cd Length: 52  Bit Score: 82.84  E-value: 2.38e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 519664503   9 YDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPNAVARGLAS 60
Cdd:cd01392    1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
PBP1_AglR_RafR-like cd06271
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ...
75-322 4.45e-19

ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380495 [Multi-domain]  Cd Length: 264  Bit Score: 85.17  E-value: 4.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  75 NMYFAQLARGIDDVATMYKYNIILTnSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTPIVFAGSVDEE 154
Cdd:cd06271   14 NGTVSE*VSGITEEAGTTGYHLLVW-PFEEAES*VPIRDLVETGSADGVILSEIEPNDPRVQFLTKQNFPFVAHGRSD*P 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 155 DLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAInGKFRLKGYKQALKSAGIPydeKLVFETDDTYKTGTLLQP 234
Cdd:cd06271   93 IGHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYSP-HDRRLQGYVRA*RDAGLT---GYPLDADTTLEAGRAAAQ 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 235 ALMA--VNATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTK-LTEMVRPKMSSITQPLYDIGAVAMRLLTKLMH 311
Cdd:cd06271  169 RLLAlsPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPfLGAMITPPLTTVHAPIAEAGRELAKALLARID 248
                        250
                 ....*....|.
gi 519664503 312 NEPVDEKNVLL 322
Cdd:cd06271  249 GEDPETLQVLV 259
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
53-330 2.11e-17

ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 81.12  E-value: 2.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  53 AVARGLASKKTTTVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEING 132
Cdd:COG1879   23 AAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 133 kLREEFKRTK---TPIV-FAGSVDEEDLYARVNIDYVA----AVQEEVKNLIDRGNrrVAFVCGPLeQAINGKFRLKGYK 204
Cdd:COG1879  103 -LAPALKKAKaagIPVVtVDSDVDGSDRVAYVGSDNYAagrlAAEYLAKALGGKGK--VAILTGSP-GAPAANERTDGFK 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 205 QALKSAGipyDEKLV------FETDDTY-KTGTLLQ--PALMAVnataaMVTDDELAAGIMNGMSDADVKvpDDFEIITS 275
Cdd:COG1879  179 EALKEYP---GIKVVaeqyadWDREKALeVMEDLLQahPDIDGI-----FAANDGMALGAAQALKAAGRK--GDVKVVGF 248
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 519664503 276 NDTK--LTEMVRPKMS-SITQPLYDIGAVAMRLLTKLMHNEPVdEKNVLLPYGLMKRE 330
Cdd:COG1879  249 DGSPeaLQAIKDGTIDaTVAQDPYLQGYLAVDAALKLLKGKEV-PKEILTPPVLVTKE 305
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
66-326 8.40e-17

Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems; Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor; in general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor.


Pssm-ID: 380479 [Multi-domain]  Cd Length: 265  Bit Score: 78.83  E-value: 8.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  66 VGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGK-LREEFKRTKTP 144
Cdd:cd01537    2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAgVAEKARGQNVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFagsVDEEDLYARvNIDYVAAVQEE-----VKNLIDRGNRRVAFVCGPLEQaINGKFRLKGYKQALKSAGIPYDEKLV 219
Cdd:cd01537   82 VVF---FDKEPSRYD-KAYYVITDSKEggiiqGDLLAKHGHIQIVLLKGPLGH-PDAEARLAGVIKELNDKGIKTEQLQL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 220 FETD-DTYKTGTLLQPALMAVNA-TAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYD 297
Cdd:cd01537  157 DTGDwDTASGKDKMDQWLSGPNKpTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANN 236
                        250       260
                 ....*....|....*....|....*....
gi 519664503 298 IGAVAMRLLTKLMHNEPVDEKNVLLPYGL 326
Cdd:cd01537  237 LGKTTFDLLLNLADNWKIDNKVVRVPYVL 265
PBP1_RafR-like cd20009
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ...
70-321 1.99e-16

Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380664 [Multi-domain]  Cd Length: 266  Bit Score: 77.96  E-value: 1.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  70 VPDVTNMYFAQLARGIDDV--ATMYKYNIILTNSDSNNEKEVK-VLNTLLSkqvDGIIFMGNEIN----GKLREE----- 137
Cdd:cd20009    8 TEDEIDGFTSQLISGISEAlrGTPYHLVVTPEFPGDDPLEPVRyIVENRLA---DGIIISHTEPQdprvRYLLERgfpfv 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 138 -FKRTKTPIVfagsvdeedlYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQAiNGKFRLKGYKQALKSAGIPYDE 216
Cdd:cd20009   85 tHGRTELSTP----------HAYFDFDNEAFAYEAVRRLAARGRRRIALVAPPRELT-YAQHRLRGFRRALAEAGLEVEP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 217 KLVFETDDTYKTGTLLQPALMAVNATA-AMVTDDELAA-GIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQP 294
Cdd:cd20009  154 LLIVTLDSSAEAIRAAARRLLRQPPRPdGIICASEIAAlGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYED 233
                        250       260
                 ....*....|....*....|....*..
gi 519664503 295 LYDIGAVAMRLLTKLMHNEPVDEKNVL 321
Cdd:cd20009  234 IEEAGRFLAEALLRRIEGEPAEPLQTL 260
PBP1_FruR cd06274
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ...
65-317 9.62e-16

ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs; Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to members of the type 1 periplasmic binding protein superfamily. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor


Pssm-ID: 380498 [Multi-domain]  Cd Length: 264  Bit Score: 75.71  E-value: 9.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTKTP 144
Cdd:cd06274    1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPSTPPDDIYYLCQAAGLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 145 IVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVCGPLEQ-AINGkfRLKGYKQALKSAGIPYDEKLVFETD 223
Cdd:cd06274   81 VVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPELpSTAE--RIRGFRAALAEAGITEGDDWILAEG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 224 DTYKTGTLLQPALMAVNAT---AAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPLYDIGA 300
Cdd:cd06274  159 YDRESGYQLMAELLARLGGlpqALFTSSLTLLEGVLRFLRERLGAIPSDLVLGTFDDHPLLDFLPNPVDSVRQDHDEIAE 238
                        250
                 ....*....|....*..
gi 519664503 301 VAMRLLTKLMHNEPVDE 317
Cdd:cd06274  239 HAFELLDALIEGQPEPG 255
LacI pfam00356
Bacterial regulatory proteins, lacI family;
7-52 1.92e-15

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 69.20  E-value: 1.92e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 519664503    7 TIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEKLDYRPN 52
Cdd:pfam00356   1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
PBP1_hexuronate_repressor-like cd06272
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ...
65-309 8.84e-15

ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and close homologs, all members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and its close homologs from other bacteria, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380496 [Multi-domain]  Cd Length: 266  Bit Score: 73.18  E-value: 8.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTN-MYFAQLARGIDDVATMYKYNIILTNsdsnneKEVKVLNTLLSK------QVDGIIFMGNEINGKLREE 137
Cdd:cd06272    1 TIGLYWPSVGErVALTRLLSGINEAISKQGYNINLSI------CPYKVGHLCTAKglfsenRFDGVIVFGISDSDIEYLN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 138 FKRTKTPIVFAGSvdEEDLYARVNIDYVAAVQEEVKNLIDRGNRRVAFVcGPLEQAINGKFRLKGYKQALKSAGIPYDEK 217
Cdd:cd06272   75 KNKPKIPIVLYNR--ESPKYSTVNVDNEKAGRLAVLLLIQKGHKSIAYI-GNPNSNRNQTLRGKGFIETCEKHGIHLSDS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 218 LVFETDDTYKTGTLLQPALMAVN--ATAAMVTDDELAAGIMNGMSDADVKVPDDFEIITSNDTKLTEMVRPKMSSITQPL 295
Cdd:cd06272  152 IIDSRGLSIEGGDNAAKKLLKKKtlPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPI 231
                        250
                 ....*....|....
gi 519664503 296 YDIGAVAMRLLTKL 309
Cdd:cd06272  232 EKIAEESLRLILKL 245
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
63-330 1.62e-14

Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).


Pssm-ID: 395423 [Multi-domain]  Cd Length: 281  Bit Score: 72.54  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   63 TTTVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEING-KLREEFKRT 141
Cdd:pfam00532   1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSGdDITAKAEGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  142 KTPIVFAG--SVDEEDLYARVNIDYVAAvQEEVKNLIDRGNRRVAFVCGPLEQAINGKFRLKGYKQALKSAGIPYDEKLV 219
Cdd:pfam00532  81 GIPVIAADdaFDNPDGVPCVMPDDTQAG-YESTQYLIAEGHKRPIAVMAGPASALTARERVQGFMAALAAAGREVKIYHV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  220 FETDDTYKTGTLLQPALMAVNAT-AAMVTD-DELAAGIMNGMSDA-DVKVPDDFEIITSNDTKLTEMVRPKMSSITQ--- 293
Cdd:pfam00532 160 ATGDNDIPDAALAANAMLVSHPTiDAIVAMnDEAAMGAVRALLKQgRVKIPDIVGIGINSVVGFDGLSKAQDTGLYLspl 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 519664503  294 -----PLYDIG-AVAMRLLTKLMHNEPVDEkNVLLPYGLMKRE 330
Cdd:pfam00532 240 tviqlPRQLLGiKASDMVYQWIPKFREHPR-VLLIPRDFFKET 281
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
65-326 4.70e-14

periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.


Pssm-ID: 380478 [Multi-domain]  Cd Length: 268  Bit Score: 71.06  E-value: 4.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEING--KLREEFKRTK 142
Cdd:cd01536    1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEAlvPAVKKANAAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 143 TPIVFAGSV--DEEDLYARVNIDYVAAVQEE----VKNLIDRGNrrVAFVCGPLEQAiNGKFRLKGYKQALKSAGipyDE 216
Cdd:cd01536   81 IPVVAVDTDidGGGDVVAFVGTDNYEAGKLAgeylAEALGGKGK--VAILEGPPGSS-TAIDRTKGFKEALKKYP---DI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 217 KLVFETD---DTYKTGTLLQPALMA---VNATAAMvtDDELAAGIMNGMSDA----DVKV------PDDFEIITSNDTKL 280
Cdd:cd01536  155 EIVAEQPanwDRAKALTVTENLLQAnpdIDAVFAA--NDDMALGAAEALKAAgrtgDIKIvgvdgtPEALKAIKDGELDA 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 519664503 281 TemvrpkmssITQPLYDIGAVAMRLLTKLMHNEPVdEKNVLLPYGL 326
Cdd:cd01536  233 T---------VAQDPYLQGYLAVEAAVKLLNGEKV-PKEILTPVTL 268
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
65-330 1.49e-12

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 67.00  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIF--MGNEINGKLREEFKRTK 142
Cdd:cd06319    1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIIspTNSSAAPTVLDLANEAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 143 TPIVFAGSVDEEDLY-----------ARVNIDYVAavqEEVKNLIDRGNRRVAFVCGPleQAINGKFRLKGYKQALKSAG 211
Cdd:cd06319   81 IPVVIADIGTGGGDYvsyiisdnydgGYQAGEYLA---EALKENGWGGGSVGIIAIPQ--SRVNGQARTAGFEDALEEAG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 212 I-PYDEKLV--FETDDTYKTGTLLQPALMAVNATAAMVtdDELAAGIMNGMSDADVKvpDDFEIITSN-DTKLTEMVRPK 287
Cdd:cd06319  156 VeEVALRQTpnSTVEETYSAAQDLLAANPDIKGIFAQN--DQMAQGALQAIEEAGRT--GDILVVGFDgDPEALDLIKDG 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 519664503 288 --MSSITQPLYDIGAVAMRLLTKLMHNEPVDEKNVLLPYGLMKRE 330
Cdd:cd06319  232 klDGTVAQQPFGMGARAVELAIQALNGDNTVEKEIYLPVLLVTSE 276
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
66-310 2.63e-10

Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433182 [Multi-domain]  Cd Length: 259  Bit Score: 60.02  E-value: 2.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503   66 VGVIVPDVTNMYFAQLARGIDDVATMYKYN-IILTNSDSNNEKEVKVLNTLLSKQVDGIIFM---GNEINGKLrEEFKRT 141
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEvIVVGPAEADAAEQVAQIEDAIAQGVDAIIVApvdPTALAPVL-KKAKDA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  142 KTPIVF--AGSVDEEDLYArVNIDYVAAVQEEVKNLIDR--GNRRVAFVCGPLEQAiNGKFRLKGYKQALKS--AGIPYd 215
Cdd:pfam13407  80 GIPVVTfdSDAPSSPRLAY-VGFDNEAAGEAAGELLAEAlgGKGKVAILSGSPGDP-NANERIDGFKKVLKEkyPGIKV- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  216 EKLVFETDDTYKTGTLLQPALMAVNAT---AAMVTDDELAAGIMNGMSDADVKvpdDFEIITSNDT---KLTEMVRPKMS 289
Cdd:pfam13407 157 VAEVEGTNWDPEKAQQQMEALLTAYPNpldGIISPNDGMAGGAAQALEAAGLA---GKVVVTGFDAtpeALEAIKDGTID 233
                         250       260
                  ....*....|....*....|..
gi 519664503  290 -SITQPLYDIGAVAMRLLTKLM 310
Cdd:pfam13407 234 aTVLQDPYGQGYAAVELAAALL 255
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
65-321 2.65e-08

periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.


Pssm-ID: 380532 [Multi-domain]  Cd Length: 285  Bit Score: 54.15  E-value: 2.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEING--KLREEFKRTK 142
Cdd:cd06309    1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGwdPVLKEAKDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 143 TP-IVFAGSVDEED--LYA-RVNIDYVA----AVQEEVKNL-IDRGNrrVAFVCGPLEQ--AINgkfRLKGYKQALKSAG 211
Cdd:cd06309   81 IPvILVDRTIDGEDgsLYVtFIGSDFVEegrrAAEWLVKNYkGGKGN--VVELQGTAGSsvAID---RSKGFREVIKKHP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 212 ipyDEKLVFETDDTYKTGT---LLQPALMAVNATAAMV--TDDELAAGIMNGMSDADVKVPDDFEIITSNDTK--LTEMV 284
Cdd:cd06309  156 ---NIKIVASQSGNFTREKgqkVMENLLQAGPGDIDVIyaHNDDMALGAIQALKEAGLKPGKDVLVVGIDGQKdaLEAIK 232
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 519664503 285 RPKMSS--ITQPLYdiGAVAMRLLTKLMHNEPVDEKNVL 321
Cdd:cd06309  233 AGELNAtvECNPLF--GPTAFDTIAKLLAGEKVPKLIIV 269
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
77-269 1.19e-05

monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380621 [Multi-domain]  Cd Length: 278  Bit Score: 46.16  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  77 YFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLREEFKRTK---TPIVFAGSVDE 153
Cdd:cd19966   14 FWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGAYTPLIEAAKkagIIVTSFNTDLP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 154 EDLYARVNIDYVAAVQEEV-----KNLIDRGNRR---VAFVCGPLEQAINGKFRLKGYKQALKSAGIPYDeklVFETDDT 225
Cdd:cd19966   94 KLEYGDCGLGYVGADLYAAgytlaKELVKRGGLKtgdRVFVPGLLPGQPYRVLRTKGVIDALKEAGIKVD---YLEISLE 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 519664503 226 YKTGTLLQPA----LMAVNATAAMVTD-DELAAGIMNGMSDADVKvPDD 269
Cdd:cd19966  171 PNKPAEGIPVmtgyLAANPDVKAIVGDgGGLTANVAKYLKAAGKK-PGE 218
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
65-320 1.71e-04

periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).


Pssm-ID: 380537 [Multi-domain]  Cd Length: 271  Bit Score: 42.57  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILT-NSDSNNEKEVKVLNTLLSKQVDGIIFMGNE-------INgKLRE 136
Cdd:cd06314    1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVgPQKSDAAEQVQLIEDLIARGVDGIAISPNDpeavtpvIN-KAAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 137 EfkrtKTPIV-FAGSVDEEDLYARVNID-YVAAVQ--EEVKNLIDRGNRRVAFVCGPleQAINGKFRLKGYKQALKsagi 212
Cdd:cd06314   80 K----GIPVItFDSDAPDSKRLAYIGTDnYEAGREagELMKKALPGGGKVAIITGGL--GADNLNERIQGFKDALK---- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 213 pydEKLVFETDDTYKTGtlLQPALMAVNATAAMVTDDELAAGIMNGMSDA--------DVKVPDDFEIITSNDTKLT-EM 283
Cdd:cd06314  150 ---GSPGIEIVDPLSDN--DDIAKAVQNVEDILKANPDLDAIFGVGAYNGpaiaaalkDAGKVGKVKIVGFDTLPETlQG 224
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 519664503 284 VRPKM--SSITQPLYDIGAVAMRLLTKLMHNEPVDEKNV 320
Cdd:cd06314  225 IKDGViaATVGQRPYEMGYLSVKLLYKLLKGGKPVPDVI 263
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
65-180 2.29e-04

monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380651 [Multi-domain]  Cd Length: 302  Bit Score: 42.23  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNI---ILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGN---EINGKLREEF 138
Cdd:cd19996    1 TIGFSNAGLGNSWRVQMIAEFEAEAAKLKKLIkelIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNsptALLPAIEKAA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 519664503 139 KRTKTPIVFAGSVDEEDLYARVNIDYVA--AVQEE--VKNLIDRGN 180
Cdd:cd19996   81 AAGIPVVLFDSGVGSDKYTAFVGVDDAAfgRVGAEwlVKQLGGKGN 126
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
65-208 1.04e-03

periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.


Pssm-ID: 380536 [Multi-domain]  Cd Length: 277  Bit Score: 40.33  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGKLR--EEFKRTK 142
Cdd:cd06313    1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPavEKAKEAG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519664503 143 TPIVFAGS-VDEEDLYARVNIDYVAAVQEEVKNLIDR--GNRRVAFVCGPLEQ--AINgkfRLKGYKQALK 208
Cdd:cd06313   81 IPLVGVNAlIENEDLTAYVGSDDVVAGELEGQAVADRlgGKGNVVILEGPIGQsaQID---RGKGIENVLK 148
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
65-125 1.73e-03

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380627 [Multi-domain]  Cd Length: 269  Bit Score: 39.35  E-value: 1.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIF 125
Cdd:cd19972    1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIY 61
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
65-327 2.11e-03

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 39.18  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMG---NEINGKLrEEFKRT 141
Cdd:cd06322    1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPvdsGGIVPAI-EAANEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 142 KTPIVFAGSV-DEEDLYARVNID-YVAAVQ--EEVKNLIDRGNRRVAFVCGPLEQAINGkfRLKGYKQAL-KSAGIPYDE 216
Cdd:cd06322   80 GIPVFTVDVKaDGAKVVTHVGTDnYAGGKLagEYALKALLGGGGKIAIIDYPEVESVVL--RVNGFKEAIkKYPNIEIVA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 217 KLVFETDDT--YK-TGTLLQ--PALMAVNATAamvtdDELAAGIMNGMSDAdvKVPDDFEII--TSNDTKLTEMVRPKM- 288
Cdd:cd06322  158 EQPGDGRREeaLAaTEDMLQanPDLDGIFAIG-----DPAALGALTAIESA--GKEDKIKVIgfDGNPEAIKAIAKGGKi 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 519664503 289 -SSITQPLYDIGAVAMRLLTKLMHNEPVdEKNVLLPYGLM 327
Cdd:cd06322  231 kADIAQQPDKIGQETVEAIVKYLAGETV-EKEILIPPKLY 269
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
65-317 3.51e-03

monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380654 [Multi-domain]  Cd Length: 313  Bit Score: 38.83  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYK-----YNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNE---INGKLRE 136
Cdd:cd19999    1 VIGVSNGYVGNEWRAQMIADFEEVAAEYKeegviSDLIVQNADADATGQISQIRNMINEGVDAILIDPVSataLNPVIEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 137 EFKRTKTPIVFAGSVDEEDLYaRVNIDYV--AAVQEE--VKNLIDRGNrrVAFVCG----PLEQAingkfRLKGYKQALK 208
Cdd:cd19999   81 AQAAGILVVSFDQPVSSPDAI-NVVIDQYkwAAIQAQwlAEQLGGKGN--IVAINGvagnPANEA-----RVKAADDVFA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503 209 SAgipYDEKLVFETD---DTYKTGTLLQPALMAVNATAAMVTDDELAAGIMNGMSDADVKVPddfeIITSND-----TKL 280
Cdd:cd19999  153 KY---PGIKVLASVPggwDQATAQQVMATLLATYPDIDGVLTQDGMAEGVLRAFQAAGKDPP----VMTGDYrkgflRKW 225
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 519664503 281 TEMVRPKMSSITQPLY-DIGAVAMRLLTKLMHNEPVDE 317
Cdd:cd19999  226 KELDLPDFESIGVVNPpGIGATALRIAVRLLQGKELKE 263
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
65-212 4.29e-03

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380544 [Multi-domain]  Cd Length: 270  Bit Score: 38.42  E-value: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYN--IILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEINGkLREEFKRTK 142
Cdd:cd06321    1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPGakVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAG-IEPAIKRAK 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519664503 143 TP--IVFAGSVDEEDLYARVNIDYVAAVQEEVKNLIDR--GNRRVAFVCGPLEQAINGkfRLKGYKQALKSA-GI 212
Cdd:cd06321   80 DAgiIVVAVDVAAEGADATVTTDNVQAGYLACEYLVEQlgGKGKVAIIDGPPVSAVID--RVNGCKEALAEYpGI 152
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
65-132 6.20e-03

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 37.74  E-value: 6.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 519664503  65 TVGVIVPDVTNMYFAQLARGIDDVATMYKYNIILTNSDSNNEKEVKVLNTLLSKQVDGIIFMGNEING 132
Cdd:cd06317    1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNG 68
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
1-46 8.25e-03

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 34.03  E-value: 8.25e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 519664503     1 MDKQTITIYDVAREASVSMATVSRVVNGNANVKPATRKKVLDVIEK 46
Cdd:smart00530   6 REEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGV 51
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH
HHS Vulnerability Disclosure